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Query: EC:3.2.1.15 (pectinase)
 2,440 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

When Bacteroides thetaiotaomicron is grown in medium which contains polygalacturonic acid (PGA) as the sole carbon source, two different polygalacturonases are produced: a PGA lyase (EC 4.2.2.2) and a PGA hydrolase (EC 3.2.1.15). Both enzymes are cell associated. The PGA hydrolase appears to be an inner membrane protein. The PGA lyase is a soluble protein that associates with membranes under certain conditions. The PGA lyase was purified to apparent homogeneity. It has a molecular weight (from sodium dodecyl sulfate-polyacrylamide gel electrophoresis) of 74,000, a pH optimum of 8.7, a pI of 7.5, and a Km for PGA of 40 to 70 micrograms/ml. It requires calcium for maximal activity. The main product of this enzyme appears to be a disaccharide that contains a delta 4,5-unsaturated galacturonic acid residue. The PGA hydrolase can be solubilized from membranes with 2% Triton X-100 and has been partially purified. It has a pH optimum of 5.4 to 5.5, a pI of 4.7 to 4.9, and a Km for PGA of 350 to 400 micrograms/ml. The main product of this enzyme appears to be galacturonic acid. The specific activities of both PGA hydrolase and PGA lyase increase at the same rate when bacteria are exposed to PGA. The two enzymes therefore appear to be similarly regulated.
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PMID:Location and characteristics of enzymes involved in the breakdown of polygalacturonic acid by Bacteroides thetaiotaomicron. 396 32

By reaction of pectin esterase (PE) from Aspergillus niger and oranges as well as lye, with 95% esterified citrus and apple pectin we prepared series of preparations with degrees of esterification between 35 and 77%. In these partial deesterified pectins the form of distribution of the free and esterified carboxyl groups has been determined from the activity coefficient gamma Ca2+ of the calcium counterions in the solutions of the corresponding calcium pectinates, from the electrostatic free enthalpy delta (Gel/N)KCa of the ion exchange Ca2+----2K+ in these systems as well as from the relative activity of the polygalacturonase reacting with sodium pectinate. The PE from A niger hydrolyzes the esterified carboxyl groups more or less randomly, in a manner similar to the effect of lye on pectin. On the other hand PE from oranges brings about block-like groupings of free carboxyl groups in the pectin molecule. The study revealed different reaction mechanisms of the pectin deesterification by pectin esterases from Aspergillus species and higher plants.
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PMID:[The distribution of free and esterified carboxyl groups within the pectin molecule after the action of pectin esterase from Aspergillus niger and oranges]. 399 Jul 79

A strain of Bacillus pumilus produced an extracellular pectic enzyme with polygalacturonic acid as the substrate. This enzyme, with optimal activity at pH 8.0 to 8.5, produced reaction products that strongly absorbed light at 232 nm, indicating the presence of a pectic acid trans-eliminase (PATE). Neither pectin esterase nor polygalacturonase was detected in the cell-free culture fluid. Chromatographic examination of the end products revealed the presence of large quantities of unsaturated oligouronides unlike those found with B. polymyxa. It was found that the PATE was produced extracellularly during the negative logarithmic death phase of the organism. The filtrate from sonically treated cells did not show any activity for PATE or hydrolases for lower oligogalacturonides at any time during the growth cycle. The enzyme was inducible. Pectin, National Formulary (NF) was the best inducer, followed by polygalacturonic acid and galacturonic acid. Enzyme activity was markedly stimulated by calcium and other divalent ions. Copper and cobalt ions were inhibitory. The partially purified enzyme showed no significant activity on pectin containing a high methoxyl content (96% esterified). However, pectin NF with a lower methoxyl content (68% esterified) was attacked to a degree by the partially purified and crude enzyme preparations. The initial rate of PATE activity increased up to 60 C, about 16-fold higher than that observed at room temperature. The activation energy was calculated as 12,183 cal/mole. A protective action of calcium chloride against heat inactivation of the PATE was observed. Degradation of polygalacturonic acid by this enzyme produced several unsaturated oligouronides soon after its addition to the substrate. The major endproduct was thought to be different from that of other known PATE enzymes. Paper chromatographic studies and viscosity measurements disclosed the random cleaving nature of the enzyme an endo-PATE.
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PMID:Purification and properties of an polygalacturonic acid trans-eliminase produced by Bacillus pumilus. 512 2

An extracellular pectinolytic enzyme produced by Butyrivibrio fibrisolvens isolated from the bovine rumen was studied. The enzyme had a pH optimum of 8.0 to 8.5 and was stimulated by Ca2+ and inhibited by EDTA. The products of pectinolysis had an absorption peak at 235 nm and reacted with thiobarbituric acid, indicating a lyase type of action. The enzyme cleaved the substrates terminally from the reducing end; action on poly- and oligogalacturonates resulted in the formation of an unsaturated trigalacturonate. The enzyme was classified as an exopectate lyase (EC 4.2.2.9). A pectinesterase was also produced by B. fibrisolvens but polygalacturonase was not detected.
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PMID:An exopectate lyase of Butyrivibrio fibrisolvens from the bovine rumen. 715 60

The characteristic features of the pectins present in the walls of immature fibre cells of the hypocotyl of flax seedlings have been studied by a combination of three subtractive methods (treatment with boiling water, calcium chelator, and free endopolygalacturonase), three staining reactions (periodic acid-thiocarbohydrazide-silver, Ruthenium Red, and ferric hydroxylamine) and labelling with an endopolygalacturonase-gold probe. The primary wall and the periphery of the tricellular junctions were shown to contain pectic molecules made of blocks either with free acidic functions or methyl-esterified, these molecules being removed from the wall by splitting alpha (1-4) linkages. On the contrary, the pectic molecules in the core of the tricellular junctions were mainly with free acidic groups, but with an appreciable acetylesterification of their hydroxyl groups; and they were linked with one another chiefly by calcium bonds. This unexpected constitution of the core of the tricellular junctions may be considered to be an early marker of the cells destined to give rise to the fibre bundles of the mature plant.
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PMID:Polysaccharide distribution in the cellular junctions of immature fibre cells of flax seedlings. 751 66

The secreted nodulation-signaling protein NodO was purified from the supernatant of cultures of Rhizobium leguminosarum biovar viciae. The native protein has a M(r) of approximately 67,000, suggesting that it exists as a dimer since the DNA sequence predicts a M(r) of 30,002. Pure NodO protein had no protease, pectinase, or cellulase activity, and no binding was observed to lipooligosaccharide nodulation factors. Although NodO is relatively hydrophilic, it appeared to insert into liposomes and was protected by liposomes from proteolytic cleavage. When added to planar lipid bilayers, NodO formed cation-selective channels that allowed the movement of monovalent cations (K+ and Na+) across the membrane. NodO is a Ca(2+)-binding protein; in the presence of high concentrations of Ca2+, channel activity was reduced. We hypothesize that NodO plays a role in nodulation signaling by stimulating uptake of nodulation factors or by forming cation-specific channels that function synergistically with the proposed lipooligosaccharide-induced depolarization of the plasma membrane of leguminous plants.
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PMID:The nodulation-signaling protein NodO from Rhizobium leguminosarum biovar viciae forms ion channels in membranes. 752 90

An exo-polygalacturonase with an isoelectric point of 4.6 and an apparent molecular weight of 45 kDa was isolated from apple tissue decayed by Botrytis cinerea. This isozyme had a similar isoelectric point, optimum pH, and mode of action as an isozyme produced in liquid culture by B. cinerea. The enzyme produced in the decayed tissue was less sensitive to lower pH and less inhibited by CaCl2, MgCl2, or NaCl than the enzyme produced in culture. Such changes in the properties of the enzyme produced in infected tissue could have been essential for the pathogen's successful colonization of the host tissue. Among the cations studied, calcium was the best inhibitor of PG activity.
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PMID:Polygalacturonase produced in apple tissue decayed by Botrytis cinerea. 762 31

Pectinolytic enzymes of four rumen fungi have been described. Three fungal species were monocentric Neocallimastix spp. H15, JL3 and OC2, and one isolate was a polycentric strain of Orpinomyces joyonii, A4. They differed in degree of pectin degradation and utilization. Only the strain Neocallimastix sp. H15 and partially Orpinomyces joyonii A4 were able to utilize pectin to a higher extent. The most important pectinolytic activity in all these isolates represented pectin lyase (EC 4.2.2.10) and polygalacturonase (EC 3.2.1.15). Their specific activities were in the range of 100-900 and 10-450 micrograms galacturonic acid h-1 mg protein-1 for pectin lyase and polygalacturonase, respectively. Polygalacturonase, located mainly in the endocellular fraction, was inhibited by calcium ions and had the main pH optimum at pH 6.0. All strains produced pectate lyase (EC 4.2.2.2). None of the strains tested produced pectinesterase (EC 3.1.1.11).
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PMID:Pectinolytic enzymes of anaerobic fungi. 776 33

We extended our previous investigations of enzymatic hydrolysis of polysaccharides in orange peel by commercial cellulase and pectinase enzymes to higher, more practical concentrations of orange peel solids. High yields of saccharification could be maintained even at substrate concentrations as high as 22-23%, but the rates of solubilization and saccharification decreased 2-3-fold. We also tested the fermentability of these hydrolysates by the yeast Saccharomyces cerevisiae, which revealed the presence of inhibitory compounds. These compounds could be removed by the filtration of hydrolyzed peel. Successful fermentations of filtered hydrolysates were achieved after pH adjustment with calcium carbonate.
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PMID:Production of ethanol from enzymatically hydrolyzed orange peel by the yeast Saccharomyces cerevisiae. 801 Jul 64

The precipitation of alginate by Ca2+ at pH 3.8 was found to occur concomitantly with the precipitation of endo-polygalacturonase from Aspergillus niger. Under optimum conditions, 92% of the enzyme activity was precipitated. The enzyme could be recovered from the precipitate by washing with 0.5 M NaCl/0.2 M Ca2+. All the precipitated endo-polygalacturonase activity could be recovered in this way. The enzyme thus obtained was purified 10-fold. A comparison of SDS/PAGE gel patterns of the crude preparation and enzyme purified by the affinity precipitation also showed a significant purification of the enzyme.
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PMID:Purification of endo-polygalacturonase by affinity precipitation using alginate. 829 9


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